ArticleAutophagy2021
Membrane dynamics and protein targets of lipid droplet microautophagy during ER stress-induced proteostasis in the budding yeast,
Article in Autophagy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 56 citations in OpenAlex.
- Mechanisms of Quality Control in GPI-Anchored Proteins: The Central Role of the Lipid Anchor.International journal of molecular sciences · 2026Review
- Lipophagy in disease: signaling control, organelle communication, and therapeutic opportunities.Cell communication and signaling : CCS · 2026Review
- Vacuolar transport and function of Saccharomyces cerevisiae sterol ester hydrolase Tgl1.FEBS letters · 2026Article
- Microautophagy: current understanding of its molecular mechanisms and functions.Autophagy reports · 2026Review
- Lipid droplets at the interface of plant defense and pathogen exploitation.Frontiers in plant science · 2026Review
- Dynamic Organellar Mapping in yeast reveals extensive protein localization changes during ER stress.Nature communications · 2025Article
- TOR and heat shock response pathways regulate peroxisome biogenesis during proteotoxic stress.Nature communications · 2025Article
- Investigating the effects of membrane curvature inducing proteins on lipid droplets in Saccharomyces cerevisiae.Molecular biology reports · 2025Article
- Lipidomics Reveals Differences in Lipid Composition Between Lipid Droplets and Milk Fat Globules in Dairy Goat Mammary Tissue.Animals : an open access journal from MDPI · 2025Article
- A Conserved N-Terminal Di-Arginine Motif Stabilizes Plant DGAT1 and Modulates Lipid Droplet Organization.International journal of molecular sciences · 2025Article
- The phenomenon of anhydrobiosis-structural and functional changes in yeast cells.Applied microbiology and biotechnology · 2025Review
- Evolutionary uniqueeLife · 2025Article
- Tools to Dissect Lipid Droplet Regulation, Players, and Mechanisms.ACS chemical biology · 2025Review
- Review
- Global proteomics reveals pathways of mesenchymal stem cells altered by Mycobacterium tuberculosis.Scientific reports · 2024Article
- Extending the G1 phase improves the production of lipophilic compounds in yeast by boosting enzyme expression and increasing cell size.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- General autophagy-dependent and -independent lipophagic processes collaborate to regulate the overall level of lipophagy in yeast.Autophagy · 2024Article
- MemPrep, a new technology for isolating organellar membranes provides fingerprints of lipid bilayer stress.The EMBO journal · 2024Article
- Mechanisms of autophagy and their implications in dermatological disorders.Frontiers in immunology · 2024Review
- Two Polarity-Sensitive Fluorescent Probes Based on Curcumin Analogs for Visualizing Polarity Changes in Lipid Droplets.Molecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Our previous studies reveal a mechanism for lipid droplet (LD)-mediated proteostasis in the endoplasmic reticulum (ER) whereby unfolded proteins that accumulate in the ER in response to lipid imbalance-induced ER stress are removed by LDs and degraded by microlipophagy (µLP), autophagosome-independent LD uptake into the vacuole (the yeast lysosome). Here, we show that dithiothreitol- or tunicamycin-induced ER stress also induces µLP and identify an unexpected role for vacuolar membrane dynamics in this process. All stressors studied induce vacuolar fragmentation prior to µLP. Moreover, during µLP, fragmented vacuoles fuse to form cup-shaped structures that encapsulate and ultimately take up LDs. Our studies also indicate that proteins of the endosome sorting complexes required for transport (ESCRT) are upregulated, required for µLP, and recruited to LDs, vacuolar membranes, and sites of vacuolar membrane scission during µLP. We identify possible target proteins for LD-mediated ER proteostasis. Our live-cell imaging studies reveal that one potential target (Nup159) localizes to punctate structures that colocalizes with LDs 1) during movement from ER membranes to the cytosol, 2) during microautophagic uptake into vacuoles, and 3) within the vacuolar lumen. Finally, we find that mutations that inhibit LD biogenesis, homotypic vacuolar membrane fusion or ESCRT function inhibit stress-induced autophagy of Nup159 and other ER proteins. Thus, we have obtained the first direct evidence that LDs and µLP can mediate ER stress-induced ER proteostasis, and identified direct roles for ESCRT and vacuolar membrane fusion in that process.
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